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Database: UniProt
Entry: A0A0M2RL32_9ACTN
LinkDB: A0A0M2RL32_9ACTN
Original site: A0A0M2RL32_9ACTN 
ID   A0A0M2RL32_9ACTN        Unreviewed;       828 AA.
AC   A0A0M2RL32;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=LQ51_27565 {ECO:0000313|EMBL:KKJ94702.1};
OS   Micromonospora sp. HK10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ94702.1, ECO:0000313|Proteomes:UP000034330};
RN   [1] {ECO:0000313|EMBL:KKJ94702.1, ECO:0000313|Proteomes:UP000034330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK10 {ECO:0000313|EMBL:KKJ94702.1,
RC   ECO:0000313|Proteomes:UP000034330};
RA   Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT   "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT   National park, Assam, India.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKJ94702.1}.
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DR   EMBL; JTGL01000223; KKJ94702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2RL32; -.
DR   STRING; 1538294.LQ51_27565; -.
DR   PATRIC; fig|1538294.3.peg.932; -.
DR   HOGENOM; CLU_002554_2_2_11; -.
DR   OrthoDB; 4349881at2; -.
DR   Proteomes; UP000034330; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR013587; Nitrate/nitrite_sensing.
DR   InterPro; IPR010910; Nitrate/nitrite_sensing_bac.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08376; NIT; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50906; NIT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKJ94702.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..828
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005640925"
FT   TRANSMEM        301..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..300
FT                   /note="NIT"
FT                   /evidence="ECO:0000259|PROSITE:PS50906"
FT   DOMAIN          517..622
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          626..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  87952 MW;  7EF169C3B01545B9 CRC64;
     MGSRSTRLRT KVVALLVSLA ALWAFAAWVT LQDGLNVLGV QTLDAQVAEP SESLRTALQE
     ERRMSVAYLG QPSPKQVEQL REQRRRSEEL AATFVTSARS WRARAAASDE LVQRIDEVAD
     RLDSLGPVRD EVAARSIDRG AAAAAYSGVL DSLFRMYAAL GKLDDEDIAK DTSTLTQLVR
     VRELMSQEDA LYSGVAAAGR ITDQEYILFA RLVGAQRFLA GEAIAELPAA DRDRYARMTA
     DPAFIRLRAL EDRLMKDGRP DRPLPVTAAE WQAAITPALD EQESAVLAAG DSLVGRAKPV
     AIWVIVRMVL AAGLGLIAVI ASIVVSITTA RALVRQLERL RDAAFRLANE QLPGVVERLG
     RGDQVDVARE APPLEFGADE IGQVGRAFNV VQETAIRTAV EQAELRRSVR EVFLSLARRT
     QALVHRQLTL LDAMERREHD AEELEDLFRV DHLATRMRRN AENLIVLSGS TPGRAWRRNV
     PMVDVVRGAV AEVEDYTRVK VLPLGPVSLA GRAVGDVIHL LAELIENGLS FSPPHTTVEV
     RGQLVGNGFA IEIEDRGLGM GEEELAAANH RIVDRSELNL ADAARLGLYV VSRLTERHGV
     KVQLRESAYG GTTAVVLIPR ELVTDNGPDA ETSGGFRAGA GSGEGAPVTS SVEAEAGTES
     ATVTGAAVPT AAETGLDSEP TPEPAEVAAE APRLTPSGLP ARVRRRPAPA APAGTSAGPA
     AAPGGAAEPA AVPGGAAEPA ADGDGDGSTG SGLPVRVRQA SLAPELRVET ATVAGDPDED
     TVRPPEQVRR MMTSYQSGTR RGRTDAARLL GGAQGVNAGP DPGDGQAT
//
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